We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2h21

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h21.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2h21.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h21| PDB=2h21 | SCENE= }}
{{STRUCTURE_2h21| PDB=2h21 | SCENE= }}
-
'''Structure of Rubisco LSMT bound to AdoMet'''
+
===Structure of Rubisco LSMT bound to AdoMet===
-
==Overview==
+
<!--
-
SET domain enzymes represent a distinct family of protein lysine methyltransferases in eukaryotes. Recent studies have yielded significant insights into the structural basis of substrate recognition and the product specificities of these enzymes. However, the mechanism by which SET domain methyltransferases catalyze the transfer of the methyl group from S-adenosyl-L-methionine to the lysine epsilon-amine has remained unresolved. To elucidate this mechanism, we have determined the structures of the plant SET domain enzyme, pea ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit methyltransferase, bound to S-adenosyl-L-methionine, and its non-reactive analogs Aza-adenosyl-L-methionine and Sinefungin, and characterized the binding of these ligands to a homolog of the enzyme. The structural and biochemical data collectively reveal that S-adenosyl-L-methionine is selectively recognized through carbon-oxygen hydrogen bonds between the cofactor's methyl group and an array of structurally conserved oxygens that comprise the methyl transfer pore in the active site. Furthermore, the structure of the enzyme co-crystallized with the product epsilon-N-trimethyllysine reveals a trigonal array of carbon-oxygen interactions between the epsilon-ammonium methyl groups and the oxygens in the pore. Taken together, these results establish a central role for carbon-oxygen hydrogen bonding in aligning the cofactor's methyl group for transfer to the lysine epsilon-amine and in coordinating the methyl groups after transfer to facilitate multiple rounds of lysine methylation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16682405}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16682405 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16682405}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Protein lysine methyltransferase]]
[[Category: Protein lysine methyltransferase]]
[[Category: Set domain]]
[[Category: Set domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:46:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:52:39 2008''

Revision as of 11:52, 27 July 2008

Image:2h21.png

Template:STRUCTURE 2h21

Structure of Rubisco LSMT bound to AdoMet

Template:ABSTRACT PUBMED 16682405

About this Structure

2H21 is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.

Reference

Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases., Couture JF, Hauk G, Thompson MJ, Blackburn GM, Trievel RC, J Biol Chem. 2006 Jul 14;281(28):19280-7. Epub 2006 May 8. PMID:16682405

Page seeded by OCA on Sun Jul 27 14:52:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h21"
Personal tools